7WKH
the grass carp IFNa
7WKH の概要
| エントリーDOI | 10.2210/pdb7wkh/pdb |
| 分子名称 | Interferon (2 entities in total) |
| 機能のキーワード | fish, interferon, cytokine |
| 由来する生物種 | Ctenopharyngodon idella (grass carp) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 19051.18 |
| 構造登録者 | |
| 主引用文献 | Wang, Z.,Xu, J.,Feng, J.,Wu, K.,Chen, K.,Jia, Z.,Zhu, X.,Huang, W.,Zhao, X.,Liu, Q.,Wang, B.,Chen, X.,Wang, J.,Zou, J. Structural and Functional Analyses of Type I IFNa Shed Light Into Its Interaction With Multiple Receptors in Fish. Front Immunol, 13:862764-862764, 2022 Cited by PubMed Abstract: Teleost type I interferons (IFNs) are categorized into group I and II subgroups that bind to distinct receptors to activate antiviral responses. However, the interaction between ligands and receptors has not fully been understood. In this study, the crystal structure of grass carp [ ()] IFNa has been solved at 1.58Å and consists of six helices. The IFNa displays a typical structure of type I IFNs with a straight helix F and lacks a helix element in the AB loop. Superposition modeling identified several key residues involved in the interaction with receptors. It was found that IFNa bound to cytokine receptor family B (CRFB) 1, CRFB2, and CRFB5, and the three receptors could form heterodimeric receptor complexes. Furthermore, mutation of Leu27, Glu103, Lys117, and His165 markedly decreased the phosphorylation of signal transducer and activator of transcription (STAT) 1a induced by IFNa in the (EPC) cells, and Glu103 was shown to be required for the IFNa-activated antiviral activity. Interestingly, wild-type and mutant IFNa proteins did not alter the phosphorylation levels of STAT1b. Our results demonstrate that fish type I IFNs, although structurally conserved, interact with the receptors in a manner that may differ from mammalian homologs. PubMed: 35392096DOI: 10.3389/fimmu.2022.862764 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.58 Å) |
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